ArticleThe Plant cell2020
Chloroplast Chaperonin-Mediated Targeting of a Thylakoid Membrane Protein.
Article in The Plant cell, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.
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Who cites it
12 citing papers in PubMed, 22 citations in OpenAlex.
- Article
- Article
- Proteostasis and protein quality control in chloroplasts: mechanisms and novel insights related to protein mislocalization.Journal of experimental botany · 2025Review
- A Holistic Investigation of Arabidopsis Proteomes Altered in Chloroplast Biogenesis and Retrograde Signalling Identifies PsbO as a Key Regulator of Chloroplast Quality Control.Plant, cell & environment · 2025Article
- Targeting signals required for protein sorting to sub-chloroplast compartments.Plant cell reports · 2024Review
- Membrane association of active genes organizes the chloroplast nucleoid structure.Proceedings of the National Academy of Sciences of the United States of America · 2024Article
- Chloroplast proteostasis: A story of birth, life, and death.Plant communications · 2023Review
- A proteostasis network safeguards the chloroplast proteome.Essays in biochemistry · 2022Review
- Article
- Arabidopsis mTERF9 protein promotes chloroplast ribosomal assembly and translation by establishing ribonucleoprotein interactions in vivo.Nucleic acids research · 2021Article
- Liquid-Liquid Phase Separation Phenomenon on Protein Sorting Within Chloroplasts.Frontiers in physiology · 2021Review
- Hold Me, Fold Me...or Not!The Plant cell · 2020Article
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3 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Posttranslational protein targeting requires chaperone assistance to direct insertion-competent proteins to integration pathways. Chloroplasts integrate nearly all thylakoid transmembrane proteins posttranslationally, but mechanisms in the stroma that assist their insertion remain largely undefined. Here, we investigated how the chloroplast chaperonin (Cpn60) facilitated the thylakoid integration of Plastidic type I signal peptidase 1 (Plsp1) using in vitro targeting assays. Cpn60 bound Plsp1 in the stroma. In isolated chloroplasts, the membrane integration of imported Plsp1 correlated with its dissociation from Cpn60. When the Plsp1 residues that interacted with Cpn60 were removed, Plsp1 did not integrate into the membrane. These results suggested Cpn60 was an intermediate in thylakoid targeting of Plsp1. In isolated thylakoids, the integration of Plsp1 decreased when Cpn60 was present in excess of cpSecA1, the stromal motor of the cpSec1 translocon that inserts unfolded Plsp1 into the thylakoid. An excess of cpSecA1 favored integration. Introducing Cpn60's obligate substrate RbcL displaced Cpn60-bound Plsp1; then, the released Plsp1 exhibited increased accessibility to cpSec1. These in vitro targeting experiments support a model in which Cpn60 captures and then releases insertion-competent Plsp1, whereas cpSecA1 recognizes free Plsp1 for integration. Thylakoid transmembrane proteins in the stroma can interact with Cpn60 to shield themselves from the aqueous environment.
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